Studies on components of immunotoxins: Purification of ricin and its subunits and influence of unreacted antibodies
| Autor: | Pierre Casellas, P. Gros, F.K. Jansen, H. Vidal |
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| Rok vydání: | 1985 |
| Předmět: |
Cancer Research
Ricin Antibodies Chromatography Affinity Mice chemistry.chemical_compound Affinity chromatography Immunotoxin Lectins Animals Isoelectric Point Polyacrylamide gel electrophoresis Cells Cultured Molecular mass Ricinus Isoelectric focusing Hemagglutination Tests Castor Bean In vitro Molecular Weight Plants Toxic Isoelectric point Oncology chemistry Biochemistry Protein Biosynthesis Electrophoresis Polyacrylamide Gel Isoelectric Focusing Plant Lectins |
| Zdroj: | International Journal of Cancer. 36:705-711 |
| ISSN: | 1097-0215 0020-7136 |
| DOI: | 10.1002/ijc.2910360615 |
| Popis: | Two ricins were purified from the seeds of Ricinus communis by a simple method based on affinity chromatography allowing large-scale preparations. Separation of these 2 ricins was achieved by ion-exchange chromatography and studies of purified subunits demonstrated that the 2 forms of ricin differed only in their B-chains which showed widely differing isoelectric points. The A-chains isolated from both ricins showed similar biological properties and contained 2 variants, A1 and A2, differing in their molecular weights and carbohydrate contents. These variants could be separated by affinity chromatography on Con-A-Sepharose which bound the A2 variant more tightly than A1. This property allowed us to obtain immunotoxin preparations devoid of free antibodies and to study the in vitro influence of free antibody on immunotoxin activity. |
| Databáze: | OpenAIRE |
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